Hydrophobic partitioning of proteins in aqueous two-phase systems

Enzyme and Microbial Technology

Volumn 19, Issue 7, 1996, Pages 507-517

  Hachem, F ^a   Andrews, B A ^a,b   Asenjo, J A ^a,b  

^a UNIVERSITY OF READING   (United Kingdom)

^b UNIVERSITY OF CHILE   (Chile)

Author keywords

Aqueous two phase partitioning; Chromatography; Correlation; Hydrophobicity; Solubility

Indexed keywords

AMMONIUM COMPOUNDS; COMPOSITION EFFECTS; CORRELATION METHODS; ENZYME KINETICS; HYDROPHOBIC CHROMATOGRAPHY; PRECIPITATION (CHEMICAL); SODIUM CHLORIDE; SOLUBILITY;

AQUEOUS TWO PHASE SYSTEMS; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; HYDROPHOBIC PARTITIONING; REVERSED PHASE CHROMATOGRAPHY;

PROTEINS;

AMMONIUM SULFATE; PROTEIN; SODIUM CHLORIDE;

ARTICLE; CHROMATOGRAPHY; HYDROPHOBICITY; PARTITION CHROMATOGRAPHY; PARTITION COEFFICIENT; PRECIPITATION; PROTEIN ANALYSIS; REVERSED PHASE LIQUID CHROMATOGRAPHY; SOLUBILITY;

EID: 0030589173     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)80002-D     Document Type: Article

References (30)

1. 1. Tanford, C. Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J. Am. Chem. Soc. 1962, 84, 4240-4247
2. 2. Bigelow, C. On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theor. Biol. 1967, 16, 187-211
3. 3. Lee, B. and Richards, F. M. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 1971, 55, 379-400
4. 4. Johansson, G. and Hartman, A. Partitioning of proteins in two-phase systems containing charged poly(ethylene glycol). In: Proceedings of the International Solvent Extraction Conference Vol. 1 (Thornton, J. D., Naylor, A., McKay, H. A. C., and Jeffreys, G. V. Eds.). Society of Chemistry Industry, London, 1974
5. 5. Eiteman, M. A. and Gainer, J. L. A model for the prediction of partition coefficients in aqueous two-phase systems. Bioseparation 1989, 2, 31-41
6. 6. Quarry, M. A., Grob, R. L., and Snyder, L. R. Prediction of precise isocratic retention data from two or more gradient elution runs. Analysis of some associated errors. Anal. Chem. 1986, 58, 907-917
7. 7. Scopes, R. K. Protein Purification: Principles and Practice. Springer-Verlag, New York, 1982
8. 8. Sedmak, J. J. and Grossberg, S. E. A rapid, sensitive, and versatile assay for protein using Coomassie Brilliant Blue G250. Anal. Biochem. 1977, 79, 544-552
9. 9. Melander, W. and Horvath, C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch. Biochem. Biophys. 1977, 183, 200-215
10. 10. El Rassi, Z., Lee, A. L. and Horvath, C. Reversed-phase and hydrophobic interaction chromatography of peptides and proteins. In: Separation Processes in Biotechnology (Asenjo, J. A., Ed.). Marcel Dekker, New York, 1990, 447-494
11. 11. Hachem, F. Hydrophobic behaviour of five model proteins in chromatography, precipitation, and aqueous two-phase systems. Ph.D. Thesis, University of Reading, UK, 1992
12. 12. Fausnaugh, J. L., Kennedy, L. A. and Regnier, F. E. Comparison of hydrophobic-interaction and reversed-phase chromatography of proteins. J. Chromatogr. 1984, 317, 141-155
13. 13. Chaplin, L. C. Hydrophobic interaction fast protein liquid chromatography of milk proteins. J. Chromatogr. 1986, 363, 329-335
14. 14. Diosady, L. L. and Bergen, I. High performance liquid chromatography of whey proteins. Milchwissenschaft 1980, 35(11), 671-674
15. 15. Pearce, R. R. Analysis of whey proteins by high performance liquid chromatography. Aust. J. Dairy Technol. 1983, 38, 114-117
16. 16. Green, A. A. Studies in the physical chemistry of the proteins. J Biol. Chem. 1931, XCIII (2), 495-516
17. 17. Przybycien, T. M. and Bailey, J. E. Solubility-activity relationships in the inorganic salt-induced precipitation of α-chymotrypsin. Enzyme Microb. Technol. 1989, 11, 264-276
18. 18. Stanley, P. G. Salting-out of multi-component systems with and without the use of constant final volumes. Biochim. Biophys. Acta 1963, 75, 442-444
19. 19. Dixon, M. and Webb, E. C. Enzyme fractionation by salting-out: A theoretical note. Adv. Prot. Chem. 1961, 16, 197-219
20. 20. Cascone, O., Andrews, B. A. and Asenjo, J. A. Partitioning and purification of thaumatin in aqueous two-phase systems. Enzyme Microb. Technol. 1991, 13, 629-635
21. 21. Schmidt, A. S., Ventom, A. M. and Asenjo, J. A. Partitioning and purification of α-amylase in aqueous two-phase systems. Enzyme Microb. Technol. 1994, 16, 131-142
22. 22. Hodgson, C. Two-phase aqueous systems for the separation and purification of tPA (tissue plasminogen activator). Ph.D. thesis, University of Reading, UK, 1992
23. 23. Johansson, G. Partitioning of proteins. In: Partitioning in Aqueous Two-Phase Systems: Theory, Methods, Uses and Applications in Biotechnology (Walter, H., Brooks, D. E., and Fisher, D.) Academic Press, London, 1985, 161-226
24. 24. Baskir, J. N., Hatton, T. A., and Suter, U. W. Protein partitioning in two-phase aqueous polymer systems. Biotechnol. Bioeng. 1989, 34, 541-558
25. 25. Franco, T. T., Andrews, A. T., and Asenjo, J. A. Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: Effect of surface hydrophobicity. Biotechnol. Bioeng. 1996, 49, 300-308
26. 26. Asenjo, J. A., Schmidt, A. S., Hachem, F., and Andrews, B. A. A model for predicting the partition behaviour of proteins in aqueous two-phase systems. J. Chromat. 1994, 668, 47-54
27. 27. Reitherman, R., Flanagan, S. D., and Barondes, S. H. Electromotive phenomena in partition of erythrocytes in aqueous polymer two-phase systems. Biochem. Biophys. Acta 1973, 297, 193-202
28. 28. Gaiscone, P. S. and Fisher, D. The dependence of cell partition in two-polymer aqueous phase systems on the electrostatic potential between the phases. Biochem. Soc. Trans. 1984, 12(6), 1085-1086
29. 29. Albertsson, P. A. Partition of proteins in liquid polymer-polymer two-phase systems. Nature 1958, 182, 709-711
30. 30. Sasakawa, S. and Walter, H. Partition behaviour of native proteins in aqueous dextran-poly(ethylene glycol) phase systems. Biochemistry 1972, 11, 2760-2765